crystallization papers
Agglutinin protein purified from the seeds of Abrus precatorius has a high antitumour activity and was crystallized at room temperature with polyethylene glycol 8000 as the precipitant. The agglutinin crystal diffracted to 3.45 Å and belongs to one of two possible tetragonal space groups, P41212 or P43212, with unit-cell parameters a = b = 141.91, c = 105.63 Å. The asymmetric unit contains a heterotetrameric protein molecule of molecular weight 134 kDa and has a solvent content of approximately 38%.